HEADER HYDROLASE 01-MAR-10 3LZK
TITLE THE CRYSTAL STRUCTURE OF A PROBABLY AROMATIC AMINO ACID
TITLE 2 DEGRADATION PROTEIN FROM SINORHIZOBIUM MELILOTI 1021
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FUMARYLACETOACETATE HYDROLASE FAMILY PROTEIN;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SINORHIZOBIUM MELILOTI;
SOURCE 3 ORGANISM_TAXID: 382;
SOURCE 4 STRAIN: 1021;
SOURCE 5 GENE: R02938, SMC03207;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: P15TV LIC
KEYWDS STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE INITIATIVE,
KEYWDS 2 MIDWEST CENTER FOR STRUCTURAL GENOMICS, MCSG, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.TAN,X.XU,H.CUI,A.SAVCHENKO,A.EDWARDS,A.JOACHIMIAK,MIDWEST
AUTHOR 2 CENTER FOR STRUCTURAL GENOMICS (MCSG)
REVDAT 1 16-MAR-10 3LZK 0
JRNL AUTH K.TAN,X.XU,H.CUI,S.CHIN,A.SAVCHENKO,A.EDWARDS,
JRNL AUTH 2 A.JOACHIMIAK
JRNL TITL THE CRYSTAL STRUCTURE OF A PROBABLY AROMATIC AMINO
JRNL TITL 2 ACID DEGRADATION PROTEIN FROM SINORHIZOBIUM
JRNL TITL 3 MELILOTI 1021
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.5_2)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 33.60
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.030
REMARK 3 COMPLETENESS FOR RANGE (%) : 90.2
REMARK 3 NUMBER OF REFLECTIONS : 100803
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.185
REMARK 3 FREE R VALUE : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 5055
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 33.6066 - 4.0911 0.95 10153 513 0.1416 0.1664
REMARK 3 2 4.0911 - 3.2481 0.97 10369 530 0.1687 0.2079
REMARK 3 3 3.2481 - 2.8378 0.98 10431 570 0.2061 0.2516
REMARK 3 4 2.8378 - 2.5784 0.96 10161 608 0.2139 0.2500
REMARK 3 5 2.5784 - 2.3936 0.93 9906 516 0.2099 0.2792
REMARK 3 6 2.3936 - 2.2526 0.91 9653 517 0.2159 0.2832
REMARK 3 7 2.2526 - 2.1398 0.89 9475 497 0.2266 0.2838
REMARK 3 8 2.1398 - 2.0466 0.86 9088 443 0.2301 0.2606
REMARK 3 9 2.0466 - 1.9678 0.81 8614 453 0.2403 0.2982
REMARK 3 10 1.9678 - 1.9000 0.75 7898 408 0.2715 0.3190
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.31
REMARK 3 B_SOL : 39.68
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.080
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.93
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.35200
REMARK 3 B22 (A**2) : -10.89770
REMARK 3 B33 (A**2) : 10.54560
REMARK 3 B12 (A**2) : -0.00000
REMARK 3 B13 (A**2) : 3.00260
REMARK 3 B23 (A**2) : -0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 10555
REMARK 3 ANGLE : 1.052 14300
REMARK 3 CHIRALITY : 0.071 1553
REMARK 3 PLANARITY : 0.004 1901
REMARK 3 DIHEDRAL : 16.912 3868
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): 7.5982 27.6410 34.5942
REMARK 3 T TENSOR
REMARK 3 T11: 0.3343 T22: 0.2388
REMARK 3 T33: 0.5148 T12: 0.0391
REMARK 3 T13: -0.1587 T23: -0.0016
REMARK 3 L TENSOR
REMARK 3 L11: 1.2069 L22: 1.3212
REMARK 3 L33: 0.5308 L12: -0.4368
REMARK 3 L13: -0.0296 L23: -0.2597
REMARK 3 S TENSOR
REMARK 3 S11: 0.0806 S12: -0.0234 S13: -0.3481
REMARK 3 S21: 0.0631 S22: 0.0160 S23: -0.0032
REMARK 3 S31: 0.2536 S32: 0.0281 S33: -0.1152
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): 1.0026 35.5903 4.8562
REMARK 3 T TENSOR
REMARK 3 T11: 0.6319 T22: 0.2401
REMARK 3 T33: 0.4455 T12: 0.1452
REMARK 3 T13: -0.1939 T23: -0.0903
REMARK 3 L TENSOR
REMARK 3 L11: 0.9152 L22: 1.1579
REMARK 3 L33: 0.8575 L12: -0.2755
REMARK 3 L13: -0.1225 L23: 0.0622
REMARK 3 S TENSOR
REMARK 3 S11: 0.2644 S12: 0.0891 S13: -0.3095
REMARK 3 S21: -0.6922 S22: -0.1933 S23: 0.1298
REMARK 3 S31: 0.2227 S32: -0.0015 S33: -0.0612
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN C
REMARK 3 ORIGIN FOR THE GROUP (A): -0.1490 84.2297 26.6508
REMARK 3 T TENSOR
REMARK 3 T11: 0.2605 T22: 0.2810
REMARK 3 T33: 0.2261 T12: 0.0172
REMARK 3 T13: 0.0313 T23: 0.0033
REMARK 3 L TENSOR
REMARK 3 L11: 1.8141 L22: 1.6194
REMARK 3 L33: 0.6770 L12: 0.2579
REMARK 3 L13: 0.6041 L23: -0.3167
REMARK 3 S TENSOR
REMARK 3 S11: -0.1121 S12: 0.0380 S13: 0.2058
REMARK 3 S21: 0.0222 S22: 0.0317 S23: -0.2258
REMARK 3 S31: -0.1417 S32: -0.0034 S33: 0.0687
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN D
REMARK 3 ORIGIN FOR THE GROUP (A): -22.9804 71.0196 43.9838
REMARK 3 T TENSOR
REMARK 3 T11: 0.2798 T22: 0.5084
REMARK 3 T33: 0.3011 T12: 0.0691
REMARK 3 T13: 0.1230 T23: 0.0872
REMARK 3 L TENSOR
REMARK 3 L11: 2.7424 L22: 1.2636
REMARK 3 L33: 0.7436 L12: -0.1326
REMARK 3 L13: 0.1738 L23: -0.0027
REMARK 3 S TENSOR
REMARK 3 S11: -0.0601 S12: -0.6647 S13: -0.2973
REMARK 3 S21: 0.2536 S22: 0.0574 S23: 0.3275
REMARK 3 S31: -0.0785 S32: -0.2103 S33: 0.0128
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3LZK COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-MAR-10.
REMARK 100 THE RCSB ID CODE IS RCSB057921.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-FEB-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97929
REMARK 200 MONOCHROMATOR : SI 111 CRYSTAL
REMARK 200 OPTICS : MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 107627
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 34.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.07900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 32.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.93
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.5
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.79000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.680
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXD/MLPHARE/DM/ARP/WARP/HKL3000
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.87
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M CACL2, 20% PEG3350, 1/70
REMARK 280 CHYMOTRYPSIN, PH 7.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 94.44700
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5360 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 25160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -20
REMARK 465 GLY A -19
REMARK 465 SER A -18
REMARK 465 SER A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 SER A -10
REMARK 465 SER A -9
REMARK 465 GLY A -8
REMARK 465 ARG A -7
REMARK 465 GLU A -6
REMARK 465 ASN A -5
REMARK 465 LEU A -4
REMARK 465 TYR A -3
REMARK 465 GLY A 338
REMARK 465 MET B -20
REMARK 465 GLY B -19
REMARK 465 SER B -18
REMARK 465 SER B -17
REMARK 465 HIS B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 SER B -10
REMARK 465 SER B -9
REMARK 465 GLY B -8
REMARK 465 ARG B -7
REMARK 465 GLU B -6
REMARK 465 ASN B -5
REMARK 465 LEU B -4
REMARK 465 TYR B -3
REMARK 465 PHE B -2
REMARK 465 GLY B 338
REMARK 465 MET C -20
REMARK 465 GLY C -19
REMARK 465 SER C -18
REMARK 465 SER C -17
REMARK 465 HIS C -16
REMARK 465 HIS C -15
REMARK 465 HIS C -14
REMARK 465 HIS C -13
REMARK 465 HIS C -12
REMARK 465 HIS C -11
REMARK 465 SER C -10
REMARK 465 SER C -9
REMARK 465 GLY C -8
REMARK 465 ARG C -7
REMARK 465 GLU C -6
REMARK 465 GLY C 338
REMARK 465 MET D -20
REMARK 465 GLY D -19
REMARK 465 SER D -18
REMARK 465 SER D -17
REMARK 465 HIS D -16
REMARK 465 HIS D -15
REMARK 465 HIS D -14
REMARK 465 HIS D -13
REMARK 465 HIS D -12
REMARK 465 HIS D -11
REMARK 465 SER D -10
REMARK 465 SER D -9
REMARK 465 GLY D -8
REMARK 465 ARG D -7
REMARK 465 GLU D -6
REMARK 465 ASN D -5
REMARK 465 LEU D -4
REMARK 465 TYR D -3
REMARK 465 PHE D -2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 VAL A 28 47.00 -141.32
REMARK 500 TYR A 188 -78.03 -144.89
REMARK 500 HIS A 216 55.21 -116.16
REMARK 500 LYS A 302 -68.82 -132.21
REMARK 500 ILE B 31 -60.36 -107.37
REMARK 500 ASN B 99 21.22 98.73
REMARK 500 ALA B 104 -7.91 -59.87
REMARK 500 SER B 119 45.96 -151.63
REMARK 500 TYR B 188 -75.86 -140.56
REMARK 500 PRO B 192 -169.57 -73.68
REMARK 500 HIS B 216 56.84 -102.56
REMARK 500 LEU B 269 -71.61 -74.05
REMARK 500 GLU B 270 33.28 -146.30
REMARK 500 PHE B 305 -168.53 -76.26
REMARK 500 TYR C -3 97.72 -69.02
REMARK 500 SER C 119 41.84 -154.13
REMARK 500 TYR C 188 -72.69 -146.47
REMARK 500 HIS C 216 48.19 -107.95
REMARK 500 ARG C 230 30.52 -142.56
REMARK 500 SER D 119 48.68 -144.77
REMARK 500 ASP D 147 -176.66 -68.60
REMARK 500 TYR D 188 -75.80 -138.58
REMARK 500 HIS D 216 52.74 -102.46
REMARK 500 ARG D 230 27.39 -143.57
REMARK 500 SER D 278 10.18 -68.75
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 339 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 83 OD2
REMARK 620 2 GLU C 141 OE2 80.5
REMARK 620 3 ASP C 170 OD2 81.8 97.0
REMARK 620 4 GLU C 139 OE2 154.8 90.8 75.8
REMARK 620 5 HOH C 354 O 114.4 162.8 93.9 78.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 339 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 83 OD2
REMARK 620 2 GLU D 141 OE2 85.0
REMARK 620 3 ASP D 170 OD2 82.9 99.1
REMARK 620 4 GLU D 139 OE2 153.3 94.5 70.8
REMARK 620 5 HOH D 426 O 108.7 165.8 86.5 75.0
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 339 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 141 OE2
REMARK 620 2 ASP A 83 OD2 82.8
REMARK 620 3 ASP A 170 OD2 96.2 68.9
REMARK 620 4 GLU A 139 OE2 89.1 144.5 77.8
REMARK 620 5 HOH A 427 O 167.3 109.8 88.0 80.1
REMARK 620 6 HOH A 429 O 89.3 137.7 153.4 76.3 81.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 339 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU B 141 OE2
REMARK 620 2 ASP B 83 OD2 80.8
REMARK 620 3 ASP B 170 OD2 86.7 70.9
REMARK 620 4 GLU B 139 OE2 102.8 163.8 93.4
REMARK 620 5 HOH B 400 O 94.7 54.5 124.1 139.5
REMARK 620 6 HOH B 388 O 83.3 108.2 170.0 88.0 57.9
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 339
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 339
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 339
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 339
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: APC65442 RELATED DB: TARGETDB
DBREF 3LZK A -20 338 UNP Q92LT4 Q92LT4_RHIME 1 338
DBREF 3LZK B -20 338 UNP Q92LT4 Q92LT4_RHIME 1 338
DBREF 3LZK C -20 338 UNP Q92LT4 Q92LT4_RHIME 1 338
DBREF 3LZK D -20 338 UNP Q92LT4 Q92LT4_RHIME 1 338
SEQADV 3LZK GLY A -19 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK SER A -18 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK SER A -17 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK HIS A -16 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK HIS A -15 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK HIS A -14 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK HIS A -13 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK HIS A -12 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK HIS A -11 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK SER A -10 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK SER A -9 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK GLY A -8 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK ARG A -7 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK GLU A -6 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK ASN A -5 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK LEU A -4 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK TYR A -3 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK PHE A -2 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK GLN A -1 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK GLY A 0 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK MSE A 1 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK GLY B -19 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK SER B -18 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK SER B -17 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK HIS B -16 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK HIS B -15 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK HIS B -14 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK HIS B -13 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK HIS B -12 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK HIS B -11 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK SER B -10 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK SER B -9 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK GLY B -8 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK ARG B -7 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK GLU B -6 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK ASN B -5 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK LEU B -4 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK TYR B -3 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK PHE B -2 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK GLN B -1 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK GLY B 0 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK MSE B 1 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK GLY C -19 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK SER C -18 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK SER C -17 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK HIS C -16 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK HIS C -15 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK HIS C -14 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK HIS C -13 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK HIS C -12 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK HIS C -11 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK SER C -10 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK SER C -9 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK GLY C -8 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK ARG C -7 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK GLU C -6 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK ASN C -5 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK LEU C -4 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK TYR C -3 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK PHE C -2 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK GLN C -1 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK GLY C 0 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK MSE C 1 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK GLY D -19 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK SER D -18 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK SER D -17 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK HIS D -16 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK HIS D -15 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK HIS D -14 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK HIS D -13 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK HIS D -12 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK HIS D -11 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK SER D -10 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK SER D -9 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK GLY D -8 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK ARG D -7 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK GLU D -6 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK ASN D -5 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK LEU D -4 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK TYR D -3 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK PHE D -2 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK GLN D -1 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK GLY D 0 UNP Q92LT4 EXPRESSION TAG
SEQADV 3LZK MSE D 1 UNP Q92LT4 EXPRESSION TAG
SEQRES 1 A 359 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 359 ARG GLU ASN LEU TYR PHE GLN GLY MSE LYS LEU ALA THR
SEQRES 3 A 359 LEU LYS ASP SER THR ARG ASP GLY LYS LEU VAL VAL VAL
SEQRES 4 A 359 SER LYS ASP LEU THR ARG CYS SER GLU VAL GLY HIS ILE
SEQRES 5 A 359 ALA ARG THR LEU GLN ALA ALA LEU ASP ASP TRP ALA HIS
SEQRES 6 A 359 ALA GLY PRO ARG LEU GLU ARG VAL ALA GLU GLY ILE GLU
SEQRES 7 A 359 THR GLY ALA GLN PRO THR MSE ARG PHE HIS GLU HIS ASP
SEQRES 8 A 359 ALA ALA SER PRO LEU PRO ARG ALA PHE GLN TRP ALA ASP
SEQRES 9 A 359 GLY SER ALA TYR VAL ASN HIS VAL GLU LEU VAL ARG LYS
SEQRES 10 A 359 ALA ARG ASN ALA GLU MSE PRO ALA SER PHE TRP THR ASP
SEQRES 11 A 359 PRO LEU ILE TYR GLN GLY GLY SER ASP SER PHE LEU GLY
SEQRES 12 A 359 PRO ARG ASP PRO ILE LEU MSE ALA ASP ASP ALA TRP GLY
SEQRES 13 A 359 ILE ASP MSE GLU GLY GLU ALA ALA VAL ILE VAL ASP ASP
SEQRES 14 A 359 VAL PRO MSE GLY ALA THR LEU ASP GLU ALA LYS ALA ALA
SEQRES 15 A 359 ILE ARG LEU VAL MSE LEU VAL ASN ASP VAL SER LEU ARG
SEQRES 16 A 359 GLY LEU ILE PRO GLY GLU LEU ALA LYS GLY PHE GLY PHE
SEQRES 17 A 359 TYR GLN SER LYS PRO SER SER ALA PHE SER PRO VAL ALA
SEQRES 18 A 359 VAL THR PRO GLU GLU LEU GLY GLU ALA TRP ASP GLY GLY
SEQRES 19 A 359 LYS LEU HIS LEU PRO LEU HIS VAL ASP LEU ASN GLY GLU
SEQRES 20 A 359 PRO PHE GLY ARG ALA ASN ALA GLY ILE ASP MSE THR PHE
SEQRES 21 A 359 ASP PHE PRO GLN LEU ILE VAL HIS ALA ALA ARG THR ARG
SEQRES 22 A 359 PRO LEU SER ALA GLY THR ILE ILE GLY SER GLY THR VAL
SEQRES 23 A 359 SER ASN LYS LEU GLU GLY GLY PRO GLY ARG PRO VAL SER
SEQRES 24 A 359 GLU GLY GLY ALA GLY TYR SER CYS ILE ALA GLU LEU ARG
SEQRES 25 A 359 MSE ILE GLU THR ILE GLU GLY GLY ALA PRO LYS THR GLN
SEQRES 26 A 359 PHE LEU LYS PHE GLY ASP VAL VAL ARG ILE GLU MSE LYS
SEQRES 27 A 359 ASP ARG THR GLY HIS SER ILE PHE GLY ALA ILE GLU GLN
SEQRES 28 A 359 LYS VAL GLY LYS TYR GLU ARG GLY
SEQRES 1 B 359 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 359 ARG GLU ASN LEU TYR PHE GLN GLY MSE LYS LEU ALA THR
SEQRES 3 B 359 LEU LYS ASP SER THR ARG ASP GLY LYS LEU VAL VAL VAL
SEQRES 4 B 359 SER LYS ASP LEU THR ARG CYS SER GLU VAL GLY HIS ILE
SEQRES 5 B 359 ALA ARG THR LEU GLN ALA ALA LEU ASP ASP TRP ALA HIS
SEQRES 6 B 359 ALA GLY PRO ARG LEU GLU ARG VAL ALA GLU GLY ILE GLU
SEQRES 7 B 359 THR GLY ALA GLN PRO THR MSE ARG PHE HIS GLU HIS ASP
SEQRES 8 B 359 ALA ALA SER PRO LEU PRO ARG ALA PHE GLN TRP ALA ASP
SEQRES 9 B 359 GLY SER ALA TYR VAL ASN HIS VAL GLU LEU VAL ARG LYS
SEQRES 10 B 359 ALA ARG ASN ALA GLU MSE PRO ALA SER PHE TRP THR ASP
SEQRES 11 B 359 PRO LEU ILE TYR GLN GLY GLY SER ASP SER PHE LEU GLY
SEQRES 12 B 359 PRO ARG ASP PRO ILE LEU MSE ALA ASP ASP ALA TRP GLY
SEQRES 13 B 359 ILE ASP MSE GLU GLY GLU ALA ALA VAL ILE VAL ASP ASP
SEQRES 14 B 359 VAL PRO MSE GLY ALA THR LEU ASP GLU ALA LYS ALA ALA
SEQRES 15 B 359 ILE ARG LEU VAL MSE LEU VAL ASN ASP VAL SER LEU ARG
SEQRES 16 B 359 GLY LEU ILE PRO GLY GLU LEU ALA LYS GLY PHE GLY PHE
SEQRES 17 B 359 TYR GLN SER LYS PRO SER SER ALA PHE SER PRO VAL ALA
SEQRES 18 B 359 VAL THR PRO GLU GLU LEU GLY GLU ALA TRP ASP GLY GLY
SEQRES 19 B 359 LYS LEU HIS LEU PRO LEU HIS VAL ASP LEU ASN GLY GLU
SEQRES 20 B 359 PRO PHE GLY ARG ALA ASN ALA GLY ILE ASP MSE THR PHE
SEQRES 21 B 359 ASP PHE PRO GLN LEU ILE VAL HIS ALA ALA ARG THR ARG
SEQRES 22 B 359 PRO LEU SER ALA GLY THR ILE ILE GLY SER GLY THR VAL
SEQRES 23 B 359 SER ASN LYS LEU GLU GLY GLY PRO GLY ARG PRO VAL SER
SEQRES 24 B 359 GLU GLY GLY ALA GLY TYR SER CYS ILE ALA GLU LEU ARG
SEQRES 25 B 359 MSE ILE GLU THR ILE GLU GLY GLY ALA PRO LYS THR GLN
SEQRES 26 B 359 PHE LEU LYS PHE GLY ASP VAL VAL ARG ILE GLU MSE LYS
SEQRES 27 B 359 ASP ARG THR GLY HIS SER ILE PHE GLY ALA ILE GLU GLN
SEQRES 28 B 359 LYS VAL GLY LYS TYR GLU ARG GLY
SEQRES 1 C 359 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 359 ARG GLU ASN LEU TYR PHE GLN GLY MSE LYS LEU ALA THR
SEQRES 3 C 359 LEU LYS ASP SER THR ARG ASP GLY LYS LEU VAL VAL VAL
SEQRES 4 C 359 SER LYS ASP LEU THR ARG CYS SER GLU VAL GLY HIS ILE
SEQRES 5 C 359 ALA ARG THR LEU GLN ALA ALA LEU ASP ASP TRP ALA HIS
SEQRES 6 C 359 ALA GLY PRO ARG LEU GLU ARG VAL ALA GLU GLY ILE GLU
SEQRES 7 C 359 THR GLY ALA GLN PRO THR MSE ARG PHE HIS GLU HIS ASP
SEQRES 8 C 359 ALA ALA SER PRO LEU PRO ARG ALA PHE GLN TRP ALA ASP
SEQRES 9 C 359 GLY SER ALA TYR VAL ASN HIS VAL GLU LEU VAL ARG LYS
SEQRES 10 C 359 ALA ARG ASN ALA GLU MSE PRO ALA SER PHE TRP THR ASP
SEQRES 11 C 359 PRO LEU ILE TYR GLN GLY GLY SER ASP SER PHE LEU GLY
SEQRES 12 C 359 PRO ARG ASP PRO ILE LEU MSE ALA ASP ASP ALA TRP GLY
SEQRES 13 C 359 ILE ASP MSE GLU GLY GLU ALA ALA VAL ILE VAL ASP ASP
SEQRES 14 C 359 VAL PRO MSE GLY ALA THR LEU ASP GLU ALA LYS ALA ALA
SEQRES 15 C 359 ILE ARG LEU VAL MSE LEU VAL ASN ASP VAL SER LEU ARG
SEQRES 16 C 359 GLY LEU ILE PRO GLY GLU LEU ALA LYS GLY PHE GLY PHE
SEQRES 17 C 359 TYR GLN SER LYS PRO SER SER ALA PHE SER PRO VAL ALA
SEQRES 18 C 359 VAL THR PRO GLU GLU LEU GLY GLU ALA TRP ASP GLY GLY
SEQRES 19 C 359 LYS LEU HIS LEU PRO LEU HIS VAL ASP LEU ASN GLY GLU
SEQRES 20 C 359 PRO PHE GLY ARG ALA ASN ALA GLY ILE ASP MSE THR PHE
SEQRES 21 C 359 ASP PHE PRO GLN LEU ILE VAL HIS ALA ALA ARG THR ARG
SEQRES 22 C 359 PRO LEU SER ALA GLY THR ILE ILE GLY SER GLY THR VAL
SEQRES 23 C 359 SER ASN LYS LEU GLU GLY GLY PRO GLY ARG PRO VAL SER
SEQRES 24 C 359 GLU GLY GLY ALA GLY TYR SER CYS ILE ALA GLU LEU ARG
SEQRES 25 C 359 MSE ILE GLU THR ILE GLU GLY GLY ALA PRO LYS THR GLN
SEQRES 26 C 359 PHE LEU LYS PHE GLY ASP VAL VAL ARG ILE GLU MSE LYS
SEQRES 27 C 359 ASP ARG THR GLY HIS SER ILE PHE GLY ALA ILE GLU GLN
SEQRES 28 C 359 LYS VAL GLY LYS TYR GLU ARG GLY
SEQRES 1 D 359 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 359 ARG GLU ASN LEU TYR PHE GLN GLY MSE LYS LEU ALA THR
SEQRES 3 D 359 LEU LYS ASP SER THR ARG ASP GLY LYS LEU VAL VAL VAL
SEQRES 4 D 359 SER LYS ASP LEU THR ARG CYS SER GLU VAL GLY HIS ILE
SEQRES 5 D 359 ALA ARG THR LEU GLN ALA ALA LEU ASP ASP TRP ALA HIS
SEQRES 6 D 359 ALA GLY PRO ARG LEU GLU ARG VAL ALA GLU GLY ILE GLU
SEQRES 7 D 359 THR GLY ALA GLN PRO THR MSE ARG PHE HIS GLU HIS ASP
SEQRES 8 D 359 ALA ALA SER PRO LEU PRO ARG ALA PHE GLN TRP ALA ASP
SEQRES 9 D 359 GLY SER ALA TYR VAL ASN HIS VAL GLU LEU VAL ARG LYS
SEQRES 10 D 359 ALA ARG ASN ALA GLU MSE PRO ALA SER PHE TRP THR ASP
SEQRES 11 D 359 PRO LEU ILE TYR GLN GLY GLY SER ASP SER PHE LEU GLY
SEQRES 12 D 359 PRO ARG ASP PRO ILE LEU MSE ALA ASP ASP ALA TRP GLY
SEQRES 13 D 359 ILE ASP MSE GLU GLY GLU ALA ALA VAL ILE VAL ASP ASP
SEQRES 14 D 359 VAL PRO MSE GLY ALA THR LEU ASP GLU ALA LYS ALA ALA
SEQRES 15 D 359 ILE ARG LEU VAL MSE LEU VAL ASN ASP VAL SER LEU ARG
SEQRES 16 D 359 GLY LEU ILE PRO GLY GLU LEU ALA LYS GLY PHE GLY PHE
SEQRES 17 D 359 TYR GLN SER LYS PRO SER SER ALA PHE SER PRO VAL ALA
SEQRES 18 D 359 VAL THR PRO GLU GLU LEU GLY GLU ALA TRP ASP GLY GLY
SEQRES 19 D 359 LYS LEU HIS LEU PRO LEU HIS VAL ASP LEU ASN GLY GLU
SEQRES 20 D 359 PRO PHE GLY ARG ALA ASN ALA GLY ILE ASP MSE THR PHE
SEQRES 21 D 359 ASP PHE PRO GLN LEU ILE VAL HIS ALA ALA ARG THR ARG
SEQRES 22 D 359 PRO LEU SER ALA GLY THR ILE ILE GLY SER GLY THR VAL
SEQRES 23 D 359 SER ASN LYS LEU GLU GLY GLY PRO GLY ARG PRO VAL SER
SEQRES 24 D 359 GLU GLY GLY ALA GLY TYR SER CYS ILE ALA GLU LEU ARG
SEQRES 25 D 359 MSE ILE GLU THR ILE GLU GLY GLY ALA PRO LYS THR GLN
SEQRES 26 D 359 PHE LEU LYS PHE GLY ASP VAL VAL ARG ILE GLU MSE LYS
SEQRES 27 D 359 ASP ARG THR GLY HIS SER ILE PHE GLY ALA ILE GLU GLN
SEQRES 28 D 359 LYS VAL GLY LYS TYR GLU ARG GLY
MODRES 3LZK MSE A 1 MET SELENOMETHIONINE
MODRES 3LZK MSE A 64 MET SELENOMETHIONINE
MODRES 3LZK MSE A 102 MET SELENOMETHIONINE
MODRES 3LZK MSE A 129 MET SELENOMETHIONINE
MODRES 3LZK MSE A 138 MET SELENOMETHIONINE
MODRES 3LZK MSE A 151 MET SELENOMETHIONINE
MODRES 3LZK MSE A 166 MET SELENOMETHIONINE
MODRES 3LZK MSE A 237 MET SELENOMETHIONINE
MODRES 3LZK MSE A 292 MET SELENOMETHIONINE
MODRES 3LZK MSE A 316 MET SELENOMETHIONINE
MODRES 3LZK MSE B 1 MET SELENOMETHIONINE
MODRES 3LZK MSE B 64 MET SELENOMETHIONINE
MODRES 3LZK MSE B 102 MET SELENOMETHIONINE
MODRES 3LZK MSE B 129 MET SELENOMETHIONINE
MODRES 3LZK MSE B 138 MET SELENOMETHIONINE
MODRES 3LZK MSE B 151 MET SELENOMETHIONINE
MODRES 3LZK MSE B 166 MET SELENOMETHIONINE
MODRES 3LZK MSE B 237 MET SELENOMETHIONINE
MODRES 3LZK MSE B 292 MET SELENOMETHIONINE
MODRES 3LZK MSE B 316 MET SELENOMETHIONINE
MODRES 3LZK MSE C 1 MET SELENOMETHIONINE
MODRES 3LZK MSE C 64 MET SELENOMETHIONINE
MODRES 3LZK MSE C 102 MET SELENOMETHIONINE
MODRES 3LZK MSE C 129 MET SELENOMETHIONINE
MODRES 3LZK MSE C 138 MET SELENOMETHIONINE
MODRES 3LZK MSE C 151 MET SELENOMETHIONINE
MODRES 3LZK MSE C 166 MET SELENOMETHIONINE
MODRES 3LZK MSE C 237 MET SELENOMETHIONINE
MODRES 3LZK MSE C 292 MET SELENOMETHIONINE
MODRES 3LZK MSE C 316 MET SELENOMETHIONINE
MODRES 3LZK MSE D 1 MET SELENOMETHIONINE
MODRES 3LZK MSE D 64 MET SELENOMETHIONINE
MODRES 3LZK MSE D 102 MET SELENOMETHIONINE
MODRES 3LZK MSE D 129 MET SELENOMETHIONINE
MODRES 3LZK MSE D 138 MET SELENOMETHIONINE
MODRES 3LZK MSE D 151 MET SELENOMETHIONINE
MODRES 3LZK MSE D 166 MET SELENOMETHIONINE
MODRES 3LZK MSE D 237 MET SELENOMETHIONINE
MODRES 3LZK MSE D 292 MET SELENOMETHIONINE
MODRES 3LZK MSE D 316 MET SELENOMETHIONINE
HET MSE A 1 8
HET MSE A 64 8
HET MSE A 102 8
HET MSE A 129 8
HET MSE A 138 8
HET MSE A 151 8
HET MSE A 166 8
HET MSE A 237 8
HET MSE A 292 8
HET MSE A 316 8
HET MSE B 1 8
HET MSE B 64 8
HET MSE B 102 8
HET MSE B 129 8
HET MSE B 138 8
HET MSE B 151 8
HET MSE B 166 8
HET MSE B 237 8
HET MSE B 292 8
HET MSE B 316 8
HET MSE C 1 8
HET MSE C 64 8
HET MSE C 102 8
HET MSE C 129 8
HET MSE C 138 8
HET MSE C 151 8
HET MSE C 166 8
HET MSE C 237 8
HET MSE C 292 8
HET MSE C 316 8
HET MSE D 1 8
HET MSE D 64 8
HET MSE D 102 8
HET MSE D 129 8
HET MSE D 138 8
HET MSE D 151 8
HET MSE D 166 8
HET MSE D 237 8
HET MSE D 292 8
HET MSE D 316 8
HET CA A 339 1
HET CA B 339 1
HET CA C 339 1
HET CA D 339 1
HETNAM MSE SELENOMETHIONINE
HETNAM CA CALCIUM ION
FORMUL 1 MSE 40(C5 H11 N O2 SE)
FORMUL 5 CA 4(CA 2+)
FORMUL 9 HOH *425(H2 O)
HELIX 1 1 THR A 34 ASP A 41 1 8
HELIX 2 2 ASP A 41 GLY A 59 1 19
HELIX 3 3 HIS A 67 ALA A 71 5 5
HELIX 4 4 TYR A 87 ARG A 98 1 12
HELIX 5 5 PRO A 103 THR A 108 5 6
HELIX 6 6 THR A 154 ALA A 161 1 8
HELIX 7 7 LEU A 176 GLY A 184 1 9
HELIX 8 8 THR A 202 GLY A 207 1 6
HELIX 9 9 GLU A 208 TRP A 210 5 3
HELIX 10 10 ASP A 240 ALA A 249 1 10
HELIX 11 11 PRO A 276 GLY A 280 5 5
HELIX 12 12 CYS A 286 GLY A 299 1 14
HELIX 13 13 THR B 34 ASP B 41 1 8
HELIX 14 14 ASP B 41 GLY B 59 1 19
HELIX 15 15 HIS B 67 ALA B 71 5 5
HELIX 16 16 TYR B 87 ALA B 97 1 11
HELIX 17 17 PRO B 103 THR B 108 5 6
HELIX 18 18 ASP B 131 TRP B 134 5 4
HELIX 19 19 THR B 154 ALA B 161 1 8
HELIX 20 20 LEU B 176 GLY B 184 1 9
HELIX 21 21 THR B 202 GLY B 207 1 6
HELIX 22 22 GLU B 208 TRP B 210 5 3
HELIX 23 23 ASP B 240 ALA B 249 1 10
HELIX 24 24 PRO B 276 GLY B 280 5 5
HELIX 25 25 CYS B 286 GLU B 297 1 12
HELIX 26 26 THR C 34 ASP C 41 1 8
HELIX 27 27 ASP C 41 GLY C 59 1 19
HELIX 28 28 HIS C 67 ALA C 71 5 5
HELIX 29 29 TYR C 87 ALA C 97 1 11
HELIX 30 30 PRO C 103 THR C 108 5 6
HELIX 31 31 ASP C 131 TRP C 134 5 4
HELIX 32 32 THR C 154 ALA C 161 1 8
HELIX 33 33 LEU C 176 LYS C 183 1 8
HELIX 34 34 THR C 202 GLY C 207 1 6
HELIX 35 35 GLU C 208 TRP C 210 5 3
HELIX 36 36 ASP C 240 ALA C 249 1 10
HELIX 37 37 PRO C 276 GLY C 280 5 5
HELIX 38 38 CYS C 286 GLY C 299 1 14
HELIX 39 39 THR D 34 ASP D 41 1 8
HELIX 40 40 ASP D 41 GLY D 59 1 19
HELIX 41 41 HIS D 67 ALA D 71 5 5
HELIX 42 42 TYR D 87 ARG D 98 1 12
HELIX 43 43 PRO D 103 THR D 108 5 6
HELIX 44 44 THR D 154 ALA D 161 1 8
HELIX 45 45 LEU D 176 GLY D 184 1 9
HELIX 46 46 THR D 202 GLY D 207 1 6
HELIX 47 47 GLU D 208 TRP D 210 5 3
HELIX 48 48 ASP D 240 ALA D 249 1 10
HELIX 49 49 PRO D 276 GLY D 280 5 5
HELIX 50 50 CYS D 286 GLY D 298 1 13
SHEET 1 A 5 MSE A 64 ARG A 65 0
SHEET 2 A 5 ARG A 24 GLU A 27 -1 N CYS A 25 O MSE A 64
SHEET 3 A 5 LYS A 14 VAL A 18 -1 N VAL A 17 O SER A 26
SHEET 4 A 5 LYS A 2 LEU A 6 -1 N LYS A 2 O VAL A 18
SHEET 5 A 5 ALA A 200 VAL A 201 -1 O ALA A 200 N LEU A 3
SHEET 1 B 6 ILE A 112 GLY A 115 0
SHEET 2 B 6 TRP A 81 GLY A 84 -1 N TRP A 81 O GLY A 115
SHEET 3 B 6 THR A 258 GLY A 261 1 O GLY A 261 N ALA A 82
SHEET 4 B 6 GLY A 140 VAL A 146 -1 N VAL A 144 O ILE A 260
SHEET 5 B 6 ILE A 162 ASN A 169 -1 O MSE A 166 N ALA A 143
SHEET 6 B 6 ALA A 195 PHE A 196 -1 O ALA A 195 N ASN A 169
SHEET 1 C 5 ILE A 127 MSE A 129 0
SHEET 2 C 5 ILE A 328 LYS A 334 1 O GLY A 333 N ILE A 127
SHEET 3 C 5 VAL A 311 MSE A 316 -1 N ILE A 314 O ILE A 328
SHEET 4 C 5 LEU A 219 LEU A 223 -1 N ASP A 222 O ARG A 313
SHEET 5 C 5 GLU A 226 GLY A 229 -1 O PHE A 228 N VAL A 221
SHEET 1 D 2 ILE A 136 ASP A 137 0
SHEET 2 D 2 SER A 172 LEU A 173 -1 O SER A 172 N ASP A 137
SHEET 1 E 5 MSE B 64 ARG B 65 0
SHEET 2 E 5 ARG B 24 GLU B 27 -1 N CYS B 25 O MSE B 64
SHEET 3 E 5 LYS B 14 VAL B 18 -1 N VAL B 17 O SER B 26
SHEET 4 E 5 LYS B 2 LEU B 6 -1 N LEU B 6 O LYS B 14
SHEET 5 E 5 ALA B 200 VAL B 201 -1 O ALA B 200 N LEU B 3
SHEET 1 F 6 ILE B 112 GLN B 114 0
SHEET 2 F 6 TRP B 81 GLY B 84 -1 N ASP B 83 O TYR B 113
SHEET 3 F 6 THR B 258 GLY B 261 1 O GLY B 261 N ALA B 82
SHEET 4 F 6 GLY B 140 VAL B 146 -1 N VAL B 144 O ILE B 260
SHEET 5 F 6 ILE B 162 ASN B 169 -1 O ARG B 163 N ILE B 145
SHEET 6 F 6 ALA B 195 PHE B 196 -1 O ALA B 195 N ASN B 169
SHEET 1 G 5 ILE B 127 MSE B 129 0
SHEET 2 G 5 ILE B 328 LYS B 334 1 O GLY B 333 N ILE B 127
SHEET 3 G 5 VAL B 311 GLU B 315 -1 N VAL B 312 O GLN B 330
SHEET 4 G 5 PRO B 218 LEU B 223 -1 N ASP B 222 O ARG B 313
SHEET 5 G 5 GLU B 226 ASN B 232 -1 O PHE B 228 N VAL B 221
SHEET 1 H 2 ILE B 136 ASP B 137 0
SHEET 2 H 2 SER B 172 LEU B 173 -1 O SER B 172 N ASP B 137
SHEET 1 I 5 MSE C 64 ARG C 65 0
SHEET 2 I 5 ARG C 24 GLU C 27 -1 N CYS C 25 O MSE C 64
SHEET 3 I 5 LYS C 14 VAL C 18 -1 N VAL C 17 O SER C 26
SHEET 4 I 5 LYS C 2 LEU C 6 -1 N ALA C 4 O VAL C 16
SHEET 5 I 5 ALA C 200 VAL C 201 -1 O ALA C 200 N LEU C 3
SHEET 1 J 6 ILE C 112 GLY C 115 0
SHEET 2 J 6 TRP C 81 GLY C 84 -1 N TRP C 81 O GLY C 115
SHEET 3 J 6 THR C 258 GLY C 261 1 O GLY C 261 N GLY C 84
SHEET 4 J 6 GLY C 140 VAL C 146 -1 N VAL C 144 O ILE C 260
SHEET 5 J 6 ILE C 162 ASN C 169 -1 O MSE C 166 N ALA C 143
SHEET 6 J 6 ALA C 195 PHE C 196 -1 O ALA C 195 N ASN C 169
SHEET 1 K 5 ILE C 127 MSE C 129 0
SHEET 2 K 5 ILE C 328 LYS C 334 1 O GLY C 333 N ILE C 127
SHEET 3 K 5 VAL C 311 MSE C 316 -1 N ILE C 314 O ILE C 328
SHEET 4 K 5 LEU C 219 LEU C 223 -1 N ASP C 222 O ARG C 313
SHEET 5 K 5 GLU C 226 GLY C 229 -1 O PHE C 228 N VAL C 221
SHEET 1 L 2 ILE C 136 ASP C 137 0
SHEET 2 L 2 SER C 172 LEU C 173 -1 O SER C 172 N ASP C 137
SHEET 1 M 5 MSE D 64 ARG D 65 0
SHEET 2 M 5 ARG D 24 GLU D 27 -1 N CYS D 25 O MSE D 64
SHEET 3 M 5 LYS D 14 VAL D 18 -1 N VAL D 17 O SER D 26
SHEET 4 M 5 LYS D 2 LEU D 6 -1 N LYS D 2 O VAL D 18
SHEET 5 M 5 ALA D 200 VAL D 201 -1 O ALA D 200 N LEU D 3
SHEET 1 N 6 ILE D 112 GLN D 114 0
SHEET 2 N 6 TRP D 81 GLY D 84 -1 N ASP D 83 O TYR D 113
SHEET 3 N 6 THR D 258 GLY D 261 1 O GLY D 261 N GLY D 84
SHEET 4 N 6 GLY D 140 VAL D 146 -1 N VAL D 144 O ILE D 260
SHEET 5 N 6 ILE D 162 ASN D 169 -1 O ARG D 163 N ILE D 145
SHEET 6 N 6 ALA D 195 PHE D 196 -1 O ALA D 195 N ASN D 169
SHEET 1 O 5 ILE D 127 MSE D 129 0
SHEET 2 O 5 ILE D 328 LYS D 334 1 O GLY D 333 N ILE D 127
SHEET 3 O 5 VAL D 311 MSE D 316 -1 N VAL D 312 O GLN D 330
SHEET 4 O 5 LEU D 219 LEU D 223 -1 N ASP D 222 O ARG D 313
SHEET 5 O 5 GLU D 226 GLY D 229 -1 O GLU D 226 N LEU D 223
SHEET 1 P 2 ILE D 136 ASP D 137 0
SHEET 2 P 2 SER D 172 LEU D 173 -1 O SER D 172 N ASP D 137
SHEET 1 Q 2 LYS D 268 LEU D 269 0
SHEET 2 Q 2 GLY D 272 PRO D 273 -1 O GLY D 272 N LEU D 269
LINK C GLY A 0 N MSE A 1 1555 1555 1.33
LINK C MSE A 1 N LYS A 2 1555 1555 1.33
LINK C THR A 63 N MSE A 64 1555 1555 1.33
LINK C MSE A 64 N ARG A 65 1555 1555 1.33
LINK C GLU A 101 N MSE A 102 1555 1555 1.33
LINK C MSE A 102 N PRO A 103 1555 1555 1.34
LINK C LEU A 128 N MSE A 129 1555 1555 1.33
LINK C MSE A 129 N ALA A 130 1555 1555 1.33
LINK C ASP A 137 N MSE A 138 1555 1555 1.33
LINK C MSE A 138 N GLU A 139 1555 1555 1.33
LINK C PRO A 150 N MSE A 151 1555 1555 1.33
LINK C MSE A 151 N GLY A 152 1555 1555 1.33
LINK C VAL A 165 N MSE A 166 1555 1555 1.33
LINK C MSE A 166 N LEU A 167 1555 1555 1.33
LINK C ASP A 236 N MSE A 237 1555 1555 1.33
LINK C MSE A 237 N THR A 238 1555 1555 1.33
LINK C ARG A 291 N MSE A 292 1555 1555 1.33
LINK C MSE A 292 N ILE A 293 1555 1555 1.34
LINK C GLU A 315 N MSE A 316 1555 1555 1.33
LINK C MSE A 316 N LYS A 317 1555 1555 1.33
LINK C GLY B 0 N MSE B 1 1555 1555 1.33
LINK C MSE B 1 N LYS B 2 1555 1555 1.33
LINK C THR B 63 N MSE B 64 1555 1555 1.33
LINK C MSE B 64 N ARG B 65 1555 1555 1.33
LINK C GLU B 101 N MSE B 102 1555 1555 1.32
LINK C MSE B 102 N PRO B 103 1555 1555 1.34
LINK C LEU B 128 N MSE B 129 1555 1555 1.33
LINK C MSE B 129 N ALA B 130 1555 1555 1.33
LINK C ASP B 137 N MSE B 138 1555 1555 1.33
LINK C MSE B 138 N GLU B 139 1555 1555 1.33
LINK C PRO B 150 N MSE B 151 1555 1555 1.33
LINK C MSE B 151 N GLY B 152 1555 1555 1.33
LINK C VAL B 165 N MSE B 166 1555 1555 1.33
LINK C MSE B 166 N LEU B 167 1555 1555 1.33
LINK C ASP B 236 N MSE B 237 1555 1555 1.33
LINK C MSE B 237 N THR B 238 1555 1555 1.33
LINK C ARG B 291 N MSE B 292 1555 1555 1.33
LINK C MSE B 292 N ILE B 293 1555 1555 1.33
LINK C GLU B 315 N MSE B 316 1555 1555 1.33
LINK C MSE B 316 N LYS B 317 1555 1555 1.33
LINK C GLY C 0 N MSE C 1 1555 1555 1.32
LINK C MSE C 1 N LYS C 2 1555 1555 1.33
LINK C THR C 63 N MSE C 64 1555 1555 1.32
LINK C MSE C 64 N ARG C 65 1555 1555 1.33
LINK C GLU C 101 N MSE C 102 1555 1555 1.33
LINK C MSE C 102 N PRO C 103 1555 1555 1.34
LINK C LEU C 128 N MSE C 129 1555 1555 1.33
LINK C MSE C 129 N ALA C 130 1555 1555 1.32
LINK C ASP C 137 N MSE C 138 1555 1555 1.33
LINK C MSE C 138 N GLU C 139 1555 1555 1.32
LINK C PRO C 150 N MSE C 151 1555 1555 1.33
LINK C MSE C 151 N GLY C 152 1555 1555 1.33
LINK C VAL C 165 N MSE C 166 1555 1555 1.33
LINK C MSE C 166 N LEU C 167 1555 1555 1.33
LINK C ASP C 236 N MSE C 237 1555 1555 1.33
LINK C MSE C 237 N THR C 238 1555 1555 1.33
LINK C ARG C 291 N MSE C 292 1555 1555 1.34
LINK C MSE C 292 N ILE C 293 1555 1555 1.33
LINK C GLU C 315 N MSE C 316 1555 1555 1.33
LINK C MSE C 316 N LYS C 317 1555 1555 1.33
LINK C GLY D 0 N MSE D 1 1555 1555 1.33
LINK C MSE D 1 N LYS D 2 1555 1555 1.33
LINK C THR D 63 N MSE D 64 1555 1555 1.33
LINK C MSE D 64 N ARG D 65 1555 1555 1.33
LINK C GLU D 101 N MSE D 102 1555 1555 1.33
LINK C MSE D 102 N PRO D 103 1555 1555 1.34
LINK C LEU D 128 N MSE D 129 1555 1555 1.33
LINK C MSE D 129 N ALA D 130 1555 1555 1.33
LINK C ASP D 137 N MSE D 138 1555 1555 1.33
LINK C MSE D 138 N GLU D 139 1555 1555 1.32
LINK C PRO D 150 N MSE D 151 1555 1555 1.33
LINK C MSE D 151 N GLY D 152 1555 1555 1.34
LINK C VAL D 165 N MSE D 166 1555 1555 1.33
LINK C MSE D 166 N LEU D 167 1555 1555 1.33
LINK C ASP D 236 N MSE D 237 1555 1555 1.32
LINK C MSE D 237 N THR D 238 1555 1555 1.33
LINK C ARG D 291 N MSE D 292 1555 1555 1.33
LINK C MSE D 292 N ILE D 293 1555 1555 1.33
LINK C GLU D 315 N MSE D 316 1555 1555 1.33
LINK C MSE D 316 N LYS D 317 1555 1555 1.33
LINK OD2 ASP C 83 CA CA C 339 1555 1555 2.34
LINK OD2 ASP D 83 CA CA D 339 1555 1555 2.34
LINK OE2 GLU D 141 CA CA D 339 1555 1555 2.37
LINK OE2 GLU C 141 CA CA C 339 1555 1555 2.39
LINK OE2 GLU A 141 CA CA A 339 1555 1555 2.41
LINK OD2 ASP A 83 CA CA A 339 1555 1555 2.42
LINK OD2 ASP A 170 CA CA A 339 1555 1555 2.49
LINK OD2 ASP D 170 CA CA D 339 1555 1555 2.49
LINK OD2 ASP C 170 CA CA C 339 1555 1555 2.50
LINK OE2 GLU B 141 CA CA B 339 1555 1555 2.55
LINK OE2 GLU C 139 CA CA C 339 1555 1555 2.55
LINK OD2 ASP B 83 CA CA B 339 1555 1555 2.61
LINK OE2 GLU A 139 CA CA A 339 1555 1555 2.62
LINK OD2 ASP B 170 CA CA B 339 1555 1555 2.62
LINK OE2 GLU D 139 CA CA D 339 1555 1555 2.88
LINK OE2 GLU B 139 CA CA B 339 1555 1555 2.89
LINK CA CA C 339 O HOH C 354 1555 1555 2.46
LINK CA CA B 339 O HOH B 400 1555 1555 2.47
LINK CA CA D 339 O HOH D 426 1555 1555 2.60
LINK CA CA A 339 O HOH A 427 1555 1555 2.63
LINK CA CA A 339 O HOH A 429 1555 1555 2.72
LINK CA CA B 339 O HOH B 388 1555 1555 2.82
SITE 1 AC1 6 ASP A 83 GLU A 139 GLU A 141 ASP A 170
SITE 2 AC1 6 HOH A 427 HOH A 429
SITE 1 AC2 7 ASP B 83 GLU B 139 GLU B 141 ASP B 170
SITE 2 AC2 7 LYS B 191 HOH B 388 HOH B 400
SITE 1 AC3 5 ASP C 83 GLU C 139 GLU C 141 ASP C 170
SITE 2 AC3 5 HOH C 354
SITE 1 AC4 5 ASP D 83 GLU D 139 GLU D 141 ASP D 170
SITE 2 AC4 5 HOH D 426
CRYST1 62.773 188.894 67.736 90.00 115.17 90.00 P 1 21 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.015930 0.000000 0.007486 0.00000
SCALE2 0.000000 0.005294 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016312 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
